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Conserved domains on  [gi|374253760|ref|NP_001243363|]
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ethanolamine-phosphate cytidylyltransferase isoform 3 [Homo sapiens]

Protein Classification

ethanolamine-phosphate cytidylyltransferase( domain architecture ID 1005722)

ethanolamine-phosphate cytidylyltransferase catalyzes the second step in the synthesis of phosphatidylethanolamine (PE) from ethanolamine via the CDP-ethanolamine pathway

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTZ00308 super family cl31425
ethanolamine-phosphate cytidylyltransferase; Provisional
 2-331 9.10e-138

ethanolamine-phosphate cytidylyltransferase; Provisional


The actual alignment was detected with superfamily member PTZ00308:

Pssm-ID: 140329 [Multi-domain]  Cd Length: 353  Bit Score: 395.31  E-value: 9.10e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253760   2 EIAKHKGPPVFTQEERYKMVQAIKWVDEVVPAAPYVTTLETLDKYNCDFCVHGNDITLTVDGRDTYEEVKQAGRYRECKR 81
Cdd:PTZ00308  50 EIMRNKGPPVMHQEERYEALRACKWVDEVVEGYPYTTRLEDLERLECDFVVHGDDISVDLNGRNSYQEIIDAGKFKVVKR 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253760  82 TQGVSTTDLVGRMLLVTKAHHssqemsseyreyadsfgkpphpipagdiLSSEGCSQCPGGRNPWTGVSQFLQTSQKIIQ 161
Cdd:PTZ00308 130 TEGISTTDLVGRMLLCTKSHL----------------------------LKSVDEVQLESSLFPYTPTSHCLTTSRKIVQ 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253760 162 FASGKEPQPGETVIYVAGAFDLFHIGHVDFLEKVHRLAErpYIIAGLHFDQEVNHYKGKNYPIMNLHERTLSVLACRYVS 241
Cdd:PTZ00308 182 FSNNRSPKPGDRIVYVDGSFDLFHIGHIRVLQKARELGD--YLIVGVHEDQVVNEQKGSNYPIMNLNERVLGVLSCRYVD 259

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253760 242 EVVIGAPYAVTAELLSHFKVDLVCHGKT-EIIPDRDGSDPYQEPKRRGIFRQIDSGSNLTTDLIVQRIITNRLEYEARNQ 320
Cdd:PTZ00308 260 EVVIGAPFDVTKEVIDSLHINVVVGGKFsDLVNEEGGSDPYEVPKAMGIFKEVDSGCDLTTDSIVDRVVKNRLAFLKRQA 339

                        330
                 ....*....|.
gi 374253760 321 KKEAKELAFLE 331
Cdd:PTZ00308 340 KKRAKEIKSQE 350
 
Name Accession Description Interval E-value
PTZ00308 PTZ00308
ethanolamine-phosphate cytidylyltransferase; Provisional
 2-331 9.10e-138

ethanolamine-phosphate cytidylyltransferase; Provisional


Pssm-ID: 140329 [Multi-domain]  Cd Length: 353  Bit Score: 395.31  E-value: 9.10e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253760   2 EIAKHKGPPVFTQEERYKMVQAIKWVDEVVPAAPYVTTLETLDKYNCDFCVHGNDITLTVDGRDTYEEVKQAGRYRECKR 81
Cdd:PTZ00308  50 EIMRNKGPPVMHQEERYEALRACKWVDEVVEGYPYTTRLEDLERLECDFVVHGDDISVDLNGRNSYQEIIDAGKFKVVKR 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253760  82 TQGVSTTDLVGRMLLVTKAHHssqemsseyreyadsfgkpphpipagdiLSSEGCSQCPGGRNPWTGVSQFLQTSQKIIQ 161
Cdd:PTZ00308 130 TEGISTTDLVGRMLLCTKSHL----------------------------LKSVDEVQLESSLFPYTPTSHCLTTSRKIVQ 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253760 162 FASGKEPQPGETVIYVAGAFDLFHIGHVDFLEKVHRLAErpYIIAGLHFDQEVNHYKGKNYPIMNLHERTLSVLACRYVS 241
Cdd:PTZ00308 182 FSNNRSPKPGDRIVYVDGSFDLFHIGHIRVLQKARELGD--YLIVGVHEDQVVNEQKGSNYPIMNLNERVLGVLSCRYVD 259

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253760 242 EVVIGAPYAVTAELLSHFKVDLVCHGKT-EIIPDRDGSDPYQEPKRRGIFRQIDSGSNLTTDLIVQRIITNRLEYEARNQ 320
Cdd:PTZ00308 260 EVVIGAPFDVTKEVIDSLHINVVVGGKFsDLVNEEGGSDPYEVPKAMGIFKEVDSGCDLTTDSIVDRVVKNRLAFLKRQA 339

                        330
                 ....*....|.
gi 374253760 321 KKEAKELAFLE 331
Cdd:PTZ00308 340 KKRAKEIKSQE 350
ECT cd02173
CTP:phosphoethanolamine cytidylyltransferase (ECT); CTP:phosphoethanolamine ...
 171-323 2.30e-95

CTP:phosphoethanolamine cytidylyltransferase (ECT); CTP:phosphoethanolamine cytidylyltransferase (ECT) catalyzes the conversion of phosphoethanolamine to CDP-ethanolamine as part of the CDP-ethanolamine biosynthesis pathway. ECT expression in hepatocytes is localized predominantly to areas of the cytoplasm that are rich in rough endoplasmic reticulum. Several ECTs, including yeast and human ECT, have large repetitive sequences located within their N- and C-termini.


Pssm-ID: 173924  Cd Length: 152  Bit Score: 279.91  E-value: 2.30e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253760 171 GETVIYVAGAFDLFHIGHVDFLEKVHRLaeRPYIIAGLHFDQEVNHYKGKNYPIMNLHERTLSVLACRYVSEVVIGAPYA 250
Cdd:cd02173    1 GDKVVYVDGAFDLFHIGHIEFLEKAREL--GDYLIVGVHDDQTVNEYKGSNYPIMNLHERVLSVLACRYVDEVVIGAPYV 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 374253760 251 VTAELLSHFKVDLVCHGKTEIIPD-RDGSDPYQEPKRRGIFRQIDSGSNLTTDLIVQRIITNRLEYEARNQKKE 323
Cdd:cd02173   79 ITKELIEHFKIDVVVHGKTEETPDsLDGEDPYAVPKEMGIFKEIDSGSDLTTRDIVNRIIKNRLAYEARNKKKE 152
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
 2-93 1.89e-19

Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; glycerol-3-phosphate cytidylyltransferase. It also includes putative adenylyltransferases, and FAD synthases.


Pssm-ID: 396172 [Multi-domain]  Cd Length: 134  Bit Score: 83.14  E-value: 1.89e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253760    2 EIAKHKGPPVFTQEERYKMVQAIKWVDEVVPAAPYVTTLETLDKYNCDFCVHGNDITLTV--DGRDTYEEVKQAGRYR-- 77
Cdd:pfam01467  36 EPPHKLKRPLFSAEERLEMLELAKWVDEVIVVAPWELTRELLKELNPDVLVIGADSLLDFwyELDEILGNVKLVVVVRpv 115

                          90
                  ....*....|....*....
gi 374253760   78 ---ECKRTQGVSTTDLVGR 93
Cdd:pfam01467 116 ffiPLKPTNGISSTDIRER 134
cyt_tran_rel TIGR00125
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain ...
 174-243 4.95e-15

cytidyltransferase-like domain; Protein families that contain at least one copy of this domain include citrate lyase ligase, pantoate-beta-alanine ligase, glycerol-3-phosphate cytidyltransferase, ADP-heptose synthase, phosphocholine cytidylyltransferase, lipopolysaccharide core biosynthesis protein KdtB, the bifunctional protein NadR, and a number whose function is unknown. Many of these proteins are known to use CTP or ATP and release pyrophosphate.


Pssm-ID: 272920 [Multi-domain]  Cd Length: 66  Bit Score: 68.87  E-value: 4.95e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253760  174 VIYVAGAFDLFHIGHVDFLEKVHRLAErpYIIAGLHFDQEVNHYKGKnyPIMNLHERTLSVLACRYVSEV 243
Cdd:TIGR00125   1 RVIFVGTFDPFHLGHLDLLERAKELFD--ELIVGVGSDQFVNPLKGE--PVFSLEERLEMLKALKYVDEV 66
TagD COG0615
Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family [Cell wall/membrane ...
 173-246 3.55e-13

Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family [Cell wall/membrane/envelope biogenesis]; Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family is part of the Pathway/BioSystem: Riboflavin/FAD biosynthesis


Pssm-ID: 440380 [Multi-domain]  Cd Length: 131  Bit Score: 65.51  E-value: 3.55e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 374253760 173 TVIYVAGAFDLFHIGHVDFLEKVHRLAErpYIIAGLHFDqEVNHYKGKNyPIMNLHERTLSVLACRYVSEVVIG 246
Cdd:COG0615    1 KRVITYGTFDLLHPGHINLLKRAKALGD--ELIVGVATD-EFVASKGRK-PIIPEEQRKEIVEALKYVDEVILG 70
 
Name Accession Description Interval E-value
PTZ00308 PTZ00308
ethanolamine-phosphate cytidylyltransferase; Provisional
 2-331 9.10e-138

ethanolamine-phosphate cytidylyltransferase; Provisional


Pssm-ID: 140329 [Multi-domain]  Cd Length: 353  Bit Score: 395.31  E-value: 9.10e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253760   2 EIAKHKGPPVFTQEERYKMVQAIKWVDEVVPAAPYVTTLETLDKYNCDFCVHGNDITLTVDGRDTYEEVKQAGRYRECKR 81
Cdd:PTZ00308  50 EIMRNKGPPVMHQEERYEALRACKWVDEVVEGYPYTTRLEDLERLECDFVVHGDDISVDLNGRNSYQEIIDAGKFKVVKR 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253760  82 TQGVSTTDLVGRMLLVTKAHHssqemsseyreyadsfgkpphpipagdiLSSEGCSQCPGGRNPWTGVSQFLQTSQKIIQ 161
Cdd:PTZ00308 130 TEGISTTDLVGRMLLCTKSHL----------------------------LKSVDEVQLESSLFPYTPTSHCLTTSRKIVQ 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253760 162 FASGKEPQPGETVIYVAGAFDLFHIGHVDFLEKVHRLAErpYIIAGLHFDQEVNHYKGKNYPIMNLHERTLSVLACRYVS 241
Cdd:PTZ00308 182 FSNNRSPKPGDRIVYVDGSFDLFHIGHIRVLQKARELGD--YLIVGVHEDQVVNEQKGSNYPIMNLNERVLGVLSCRYVD 259

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253760 242 EVVIGAPYAVTAELLSHFKVDLVCHGKT-EIIPDRDGSDPYQEPKRRGIFRQIDSGSNLTTDLIVQRIITNRLEYEARNQ 320
Cdd:PTZ00308 260 EVVIGAPFDVTKEVIDSLHINVVVGGKFsDLVNEEGGSDPYEVPKAMGIFKEVDSGCDLTTDSIVDRVVKNRLAFLKRQA 339

                        330
                 ....*....|.
gi 374253760 321 KKEAKELAFLE 331
Cdd:PTZ00308 340 KKRAKEIKSQE 350
PLN02406 PLN02406
ethanolamine-phosphate cytidylyltransferase
 2-326 3.17e-101

ethanolamine-phosphate cytidylyltransferase


Pssm-ID: 215227 [Multi-domain]  Cd Length: 418  Bit Score: 304.68  E-value: 3.17e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253760   2 EIAKHKGPPVFTQEERYKMVQAIKWVDEVVPAAPYVTTLETL----DKYNCDFCVHGNDITLTVDGRDTYEEVKQAGRYR 77
Cdd:PLN02406  92 EIIANKGPPVTPMHERMIMVSGVKWVDEVIPDAPYAITEEFMnklfNEYNIDYIIHGDDPCLLPDGTDAYALAKKAGRYK 171

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253760  78 ECKRTQGVSTTDLVGRMLLVTKAH--HSSQEMSSEYREYadsfgkpphpipagdilsSEGCSQCPG-GRNPWTGVSQFLQ 154
Cdd:PLN02406 172 QIKRTEGVSSTDIVGRMLLCVRERsiSDSHNHSSLQRQF------------------SHGHSQFEDgGSGSGTRVSHFLP 233

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253760 155 TSQKIIQFASGKEPQPGETVIYVAGAFDLFHIGHVDFLEKVHRLAErpYIIAGLHFDQEVNHYKGKNYPIMNLHERTLSV 234
Cdd:PLN02406 234 TSRRIVQFSNGKGPGPDARIVYIDGAFDLFHAGHVEILRLARALGD--FLLVGIHTDQTVSAHRGAHRPIMNLHERSLSV 311

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253760 235 LACRYVSEVVIGAPYAVTAELLSHFKVDLVCHGK-TEIIPDRDG-SDPYQEPKRRGIFRQIDSGSNLTTDLIVQRIITNR 312
Cdd:PLN02406 312 LACRYVDEVIIGAPWEVSKDMITTFNISLVVHGTvAENNDFLKGeDDPYAVPKSMGIFQVLESPLDITTSTIIRRIVANH 391

                        330
                 ....*....|....
gi 374253760 313 LEYEARNQKKEAKE 326
Cdd:PLN02406 392 EAYQKRNEKKAESE 405
ECT cd02173
CTP:phosphoethanolamine cytidylyltransferase (ECT); CTP:phosphoethanolamine ...
 171-323 2.30e-95

CTP:phosphoethanolamine cytidylyltransferase (ECT); CTP:phosphoethanolamine cytidylyltransferase (ECT) catalyzes the conversion of phosphoethanolamine to CDP-ethanolamine as part of the CDP-ethanolamine biosynthesis pathway. ECT expression in hepatocytes is localized predominantly to areas of the cytoplasm that are rich in rough endoplasmic reticulum. Several ECTs, including yeast and human ECT, have large repetitive sequences located within their N- and C-termini.


Pssm-ID: 173924  Cd Length: 152  Bit Score: 279.91  E-value: 2.30e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253760 171 GETVIYVAGAFDLFHIGHVDFLEKVHRLaeRPYIIAGLHFDQEVNHYKGKNYPIMNLHERTLSVLACRYVSEVVIGAPYA 250
Cdd:cd02173    1 GDKVVYVDGAFDLFHIGHIEFLEKAREL--GDYLIVGVHDDQTVNEYKGSNYPIMNLHERVLSVLACRYVDEVVIGAPYV 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 374253760 251 VTAELLSHFKVDLVCHGKTEIIPD-RDGSDPYQEPKRRGIFRQIDSGSNLTTDLIVQRIITNRLEYEARNQKKE 323
Cdd:cd02173   79 ITKELIEHFKIDVVVHGKTEETPDsLDGEDPYAVPKEMGIFKEIDSGSDLTTRDIVNRIIKNRLAYEARNKKKE 152
CCT cd02174
CTP:phosphocholine cytidylyltransferase; CTP:phosphocholine cytidylyltransferase (CCT) ...
 2-104 9.47e-64

CTP:phosphocholine cytidylyltransferase; CTP:phosphocholine cytidylyltransferase (CCT) catalyzes the condensation of CTP and phosphocholine to form CDP-choline as the rate-limiting and regulatory step in the CDP-choline pathway. CCT is unique in that its enzymatic activity is regulated by the extent of its association with membrane structures. A current model posts that the elastic stress of the bilayer curvature is sensed by CCT and this governs the degree of membrane association, thus providing a mechanism for both positive and negative regulation of activity.


Pssm-ID: 173925  Cd Length: 150  Bit Score: 199.33  E-value: 9.47e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253760   2 EIAKHKGPPVFTQEERYKMVQAIKWVDEVVPAAPYVTTLETLDKYNCDFCVHGNDITLTVDGRDTYEEVKQAGRYRECKR 81
Cdd:cd02174   43 EIHKHKGPPVMTEEERYEAVRHCKWVDEVVEGAPYVTTPEFLDKYKCDYVAHGDDIYLDADGEDCYQEVKDAGRFKEVKR 122

                         90       100
                 ....*....|....*....|...
gi 374253760  82 TQGVSTTDLVGRMLLVTKAHHSS 104
Cdd:cd02174  123 TEGVSTTDLIGRILLDYRDYHRR 145
CCT cd02174
CTP:phosphocholine cytidylyltransferase; CTP:phosphocholine cytidylyltransferase (CCT) ...
 175-311 2.01e-36

CTP:phosphocholine cytidylyltransferase; CTP:phosphocholine cytidylyltransferase (CCT) catalyzes the condensation of CTP and phosphocholine to form CDP-choline as the rate-limiting and regulatory step in the CDP-choline pathway. CCT is unique in that its enzymatic activity is regulated by the extent of its association with membrane structures. A current model posts that the elastic stress of the bilayer curvature is sensed by CCT and this governs the degree of membrane association, thus providing a mechanism for both positive and negative regulation of activity.


Pssm-ID: 173925  Cd Length: 150  Bit Score: 128.84  E-value: 2.01e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253760 175 IYVAGAFDLFHIGHVDFLEKVHRLAERPYIIAGLHFDQEVNHYKGKnyPIMNLHERTLSVLACRYVSEVVIGAPYAVTAE 254
Cdd:cd02174    5 VYVDGCFDLFHYGHANALRQAKKLGPNDYLIVGVHSDEEIHKHKGP--PVMTEEERYEAVRHCKWVDEVVEGAPYVTTPE 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253760 255 LLSHFKVDLVCHGKtEIIPDRDGSDPYQEPKRRGIFRQI---DSGSnlTTDlIVQRIITN 311
Cdd:cd02174   83 FLDKYKCDYVAHGD-DIYLDADGEDCYQEVKDAGRFKEVkrtEGVS--TTD-LIGRILLD 138
cytidylyltransferase cd02170
cytidylyltransferase; The cytidylyltransferase family includes cholinephosphate ...
 2-97 6.50e-30

cytidylyltransferase; The cytidylyltransferase family includes cholinephosphate cytidylyltransferase (CCT), glycerol-3-phosphate cytidylyltransferase, RafE and phosphoethanolamine cytidylyltransferase (ECT). All enzymes catalyze the transfer of a cytidylyl group from CTP to various substrates.


Pssm-ID: 173921 [Multi-domain]  Cd Length: 136  Bit Score: 111.23  E-value: 6.50e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253760   2 EIAKHKGPPVFTQEERYKMVQAIKWVDEVVPAAPYVTTLETLDKYNcDFCVHGNDITLTVDGRDTYEEVKQAGRYREC-- 79
Cdd:cd02170   40 TVAKIKRRPILPEEQRAEVVEALKYVDEVILGHPWSYFKPLEELKP-DVIVLGDDQKNGVDEEEVYEELKKRGKVIEVpr 118

                         90
                 ....*....|....*...
gi 374253760  80 KRTQGVSTTDLVGRMLLV 97
Cdd:cd02170  119 KKTEGISSSDIIKRILEL 136
PTZ00308 PTZ00308
ethanolamine-phosphate cytidylyltransferase; Provisional
 169-309 8.26e-25

ethanolamine-phosphate cytidylyltransferase; Provisional


Pssm-ID: 140329 [Multi-domain]  Cd Length: 353  Bit Score: 102.94  E-value: 8.26e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253760 169 QPGETVIYVAGAFDLFHIGHVDFLEKVHRLAERpyIIAGLHFDQEVNHYKGKnyPIMNLHERTLSVLACRYVSEVVIGAP 248
Cdd:PTZ00308   8 KPGTIRVWVDGCFDMLHFGHANALRQARALGDE--LFVGCHSDEEIMRNKGP--PVMHQEERYEALRACKWVDEVVEGYP 83

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 374253760 249 YAVTAELLSHFKVDLVCHGKtEIIPDRDGSDPYQEPKRRGIFRQIDSGSNLTTDLIVQRII 309
Cdd:PTZ00308  84 YTTRLEDLERLECDFVVHGD-DISVDLNGRNSYQEIIDAGKFKVVKRTEGISTTDLVGRML 143
PLN02413 PLN02413
choline-phosphate cytidylyltransferase
 5-95 8.44e-25

choline-phosphate cytidylyltransferase


Pssm-ID: 215229  Cd Length: 294  Bit Score: 101.95  E-value: 8.44e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253760   5 KHKGPPVFTQEERYKMVQAIKWVDEVVPAAPYVTTLETLDKYNCDFCVHgnDITLTVD----GRDTYEEVKQAGRYRECK 80
Cdd:PLN02413  71 KYKGKTVMTEDERYESLRHCKWVDEVIPDAPWVITQEFLDKHRIDYVAH--DALPYADasgaGKDVYEFVKKIGKFKETK 148

                         90
                 ....*....|....*
gi 374253760  81 RTQGVSTTDLVGRML 95
Cdd:PLN02413 149 RTDGISTSDIIMRIV 163
cytidylyltransferase cd02170
cytidylyltransferase; The cytidylyltransferase family includes cholinephosphate ...
 172-309 1.61e-21

cytidylyltransferase; The cytidylyltransferase family includes cholinephosphate cytidylyltransferase (CCT), glycerol-3-phosphate cytidylyltransferase, RafE and phosphoethanolamine cytidylyltransferase (ECT). All enzymes catalyze the transfer of a cytidylyl group from CTP to various substrates.


Pssm-ID: 173921 [Multi-domain]  Cd Length: 136  Bit Score: 88.89  E-value: 1.61e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253760 172 ETVIYVAGAFDLFHIGHVDFLEKVHRLAErpYIIAGLHFDQEVNHYKGKnyPIMNLHERTLSVLACRYVSEVVIGAPYAV 251
Cdd:cd02170    1 MKRVYAAGTFDIIHPGHIRFLEEAKKLGD--YLIVGVARDETVAKIKRR--PILPEEQRAEVVEALKYVDEVILGHPWSY 76

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253760 252 TAELLsHFKVDLVCHGKTEIIPDrDGSDPYQEPKRRGIFRQI--DSGSNLTTDLIVQRII 309
Cdd:cd02170   77 FKPLE-ELKPDVIVLGDDQKNGV-DEEEVYEELKKRGKVIEVprKKTEGISSSDIIKRIL 134
PLN02413 PLN02413
choline-phosphate cytidylyltransferase
 163-319 4.42e-21

choline-phosphate cytidylyltransferase


Pssm-ID: 215229  Cd Length: 294  Bit Score: 91.55  E-value: 4.42e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253760 163 ASGKEPQPGETVIYVAGAFDLFHIGHVDFLEKVHRLAERPYIIAGLHFDQEVNHYKGKNypIMNLHERTLSVLACRYVSE 242
Cdd:PLN02413  18 TPSSSPSDRPVRVYADGIYDLFHFGHARSLEQAKKLFPNTYLLVGCCNDELTHKYKGKT--VMTEDERYESLRHCKWVDE 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253760 243 VVIGAPYAVTAELLSHFKVDLVCHgktEIIPDRD----GSDPYQEPKRRGIFRQIDSGSNLTTDLIVQRIITNRLEYEAR 318
Cdd:PLN02413  96 VIPDAPWVITQEFLDKHRIDYVAH---DALPYADasgaGKDVYEFVKKIGKFKETKRTDGISTSDIIMRIVKDYNQYVMR 172


                 .
gi 374253760 319 N 319
Cdd:PLN02413 173 N 173
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
 2-93 1.89e-19

Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; glycerol-3-phosphate cytidylyltransferase. It also includes putative adenylyltransferases, and FAD synthases.


Pssm-ID: 396172 [Multi-domain]  Cd Length: 134  Bit Score: 83.14  E-value: 1.89e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253760    2 EIAKHKGPPVFTQEERYKMVQAIKWVDEVVPAAPYVTTLETLDKYNCDFCVHGNDITLTV--DGRDTYEEVKQAGRYR-- 77
Cdd:pfam01467  36 EPPHKLKRPLFSAEERLEMLELAKWVDEVIVVAPWELTRELLKELNPDVLVIGADSLLDFwyELDEILGNVKLVVVVRpv 115

                          90
                  ....*....|....*....
gi 374253760   78 ---ECKRTQGVSTTDLVGR 93
Cdd:pfam01467 116 ffiPLKPTNGISSTDIRER 134
PLN02406 PLN02406
ethanolamine-phosphate cytidylyltransferase
 175-310 1.37e-16

ethanolamine-phosphate cytidylyltransferase


Pssm-ID: 215227 [Multi-domain]  Cd Length: 418  Bit Score: 80.11  E-value: 1.37e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253760 175 IYVAGAFDLFHIGHVDFLEKVHRLAERpyIIAGLHFDQEVNHYKGKnyPIMNLHERTLSVLACRYVSEVVIGAPYAVTAE 254
Cdd:PLN02406  56 VYMDGCFDMMHYGHANALRQARALGDE--LVVGVVSDEEIIANKGP--PVTPMHERMIMVSGVKWVDEVIPDAPYAITEE 131

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 374253760 255 ----LLSHFKVDLVCHGKTE-IIPdrDGSDPYQEPKRRGIFRQIDSGSNLTTDLIVQRIIT 310
Cdd:PLN02406 132 fmnkLFNEYNIDYIIHGDDPcLLP--DGTDAYALAKKAGRYKQIKRTEGVSSTDIVGRMLL 190
cyt_tran_rel TIGR00125
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain ...
 174-243 4.95e-15

cytidyltransferase-like domain; Protein families that contain at least one copy of this domain include citrate lyase ligase, pantoate-beta-alanine ligase, glycerol-3-phosphate cytidyltransferase, ADP-heptose synthase, phosphocholine cytidylyltransferase, lipopolysaccharide core biosynthesis protein KdtB, the bifunctional protein NadR, and a number whose function is unknown. Many of these proteins are known to use CTP or ATP and release pyrophosphate.


Pssm-ID: 272920 [Multi-domain]  Cd Length: 66  Bit Score: 68.87  E-value: 4.95e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253760  174 VIYVAGAFDLFHIGHVDFLEKVHRLAErpYIIAGLHFDQEVNHYKGKnyPIMNLHERTLSVLACRYVSEV 243
Cdd:TIGR00125   1 RVIFVGTFDPFHLGHLDLLERAKELFD--ELIVGVGSDQFVNPLKGE--PVFSLEERLEMLKALKYVDEV 66
TagD COG0615
Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family [Cell wall/membrane ...
 173-246 3.55e-13

Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family [Cell wall/membrane/envelope biogenesis]; Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family is part of the Pathway/BioSystem: Riboflavin/FAD biosynthesis


Pssm-ID: 440380 [Multi-domain]  Cd Length: 131  Bit Score: 65.51  E-value: 3.55e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 374253760 173 TVIYVAGAFDLFHIGHVDFLEKVHRLAErpYIIAGLHFDqEVNHYKGKNyPIMNLHERTLSVLACRYVSEVVIG 246
Cdd:COG0615    1 KRVITYGTFDLLHPGHINLLKRAKALGD--ELIVGVATD-EFVASKGRK-PIIPEEQRKEIVEALKYVDEVILG 70
TagD COG0615
Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family [Cell wall/membrane ...
 3-94 1.29e-12

Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family [Cell wall/membrane/envelope biogenesis]; Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family is part of the Pathway/BioSystem: Riboflavin/FAD biosynthesis


Pssm-ID: 440380 [Multi-domain]  Cd Length: 131  Bit Score: 63.97  E-value: 1.29e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253760   3 IAKHKGPPVFTQEERYKMVQAIKWVDEVVpaaPYVTT--LETLDKYNCDFCVHGNDITLTVDG-RDTYEEVKQAGRYREC 79
Cdd:COG0615   40 VASKGRKPIIPEEQRKEIVEALKYVDEVI---LGEEWdkFEDIEEIKPDVIVLGDDWKGDFDFlKEELEKRGIGCEVVYL 116

                         90
                 ....*....|....*
gi 374253760  80 KRTQGVSTTDLVGRM 94
Cdd:COG0615  117 PRTEGISSTKIKKRI 131
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
 176-267 1.50e-12

Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; glycerol-3-phosphate cytidylyltransferase. It also includes putative adenylyltransferases, and FAD synthases.


Pssm-ID: 396172 [Multi-domain]  Cd Length: 134  Bit Score: 63.88  E-value: 1.50e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253760  176 YVAGAFDLFHIGHVDFLEKVHRLAERPyIIAGLHFDQEVNHYKgknYPIMNLHERTLSVLACRYVSEVVIGAPYAVTAEL 255
Cdd:pfam01467   1 LFGGTFDPIHLGHLRLLEQAKELFDED-LIVGVPSDEPPHKLK---RPLFSAEERLEMLELAKWVDEVIVVAPWELTREL 76

                          90
                  ....*....|..
gi 374253760  256 LSHFKVDLVCHG 267
Cdd:pfam01467  77 LKELNPDVLVIG 88
ECT cd02173
CTP:phosphoethanolamine cytidylyltransferase (ECT); CTP:phosphoethanolamine ...
 2-95 2.16e-12

CTP:phosphoethanolamine cytidylyltransferase (ECT); CTP:phosphoethanolamine cytidylyltransferase (ECT) catalyzes the conversion of phosphoethanolamine to CDP-ethanolamine as part of the CDP-ethanolamine biosynthesis pathway. ECT expression in hepatocytes is localized predominantly to areas of the cytoplasm that are rich in rough endoplasmic reticulum. Several ECTs, including yeast and human ECT, have large repetitive sequences located within their N- and C-termini.


Pssm-ID: 173924  Cd Length: 152  Bit Score: 64.20  E-value: 2.16e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253760   2 EIAKHKGP--PVFTQEERYKMVQAIKWVDEVVPAAPYVTTLETLDKYNCDFCVHG--NDITLTVDGRDTYEEVKQAGRYR 77
Cdd:cd02173   41 TVNEYKGSnyPIMNLHERVLSVLACRYVDEVVIGAPYVITKELIEHFKIDVVVHGktEETPDSLDGEDPYAVPKEMGIFK 120

                         90
                 ....*....|....*...
gi 374253760  78 ECKRTQGVSTTDLVGRML 95
Cdd:cd02173  121 EIDSGSDLTTRDIVNRII 138
RfaE_N cd02172
N-terminal domain of RfaE; RfaE is a protein involved in the biosynthesis of ...
 169-276 3.31e-11

N-terminal domain of RfaE; RfaE is a protein involved in the biosynthesis of ADP-L-glycero-D-manno-heptose, a precursor for LPS inner core biosynthesis. RfaE is a bifunctional protein in Escherichia coli, and separate proteins in other organisms. Domain I is suggested to act in D-glycero-D-manno-heptose 1-phosphate biosynthesis, while domain II (this family) adds ADP to yield ADP-D-glycero-D-manno-heptose .


Pssm-ID: 173923 [Multi-domain]  Cd Length: 144  Bit Score: 60.51  E-value: 3.31e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253760 169 QPGETVIYVAGAFDLFHIGHVDFLEKVHRLAERpyIIAGLHFDQEVNhyKGKNYPIMNLHERTLSVLACRYVSEVVIgAP 248
Cdd:cd02172    1 QRGKTVVLCHGVFDLLHPGHVRHLQAARSLGDI--LVVSLTSDRYVN--KGPGRPIFPEDLRAEVLAALGFVDYVVL-FD 75

                         90       100
                 ....*....|....*....|....*...
gi 374253760 249 YAVTAELLSHFKVDLVCHGKTEIIPDRD 276
Cdd:cd02172   76 NPTALEIIDALQPNIYVKGGDYENPEND 103
rfaE_dom_II TIGR02199
rfaE bifunctional protein, domain II; RfaE is a protein involved in the biosynthesis of ...
 171-245 2.06e-08

rfaE bifunctional protein, domain II; RfaE is a protein involved in the biosynthesis of ADP-L-glycero-D-manno-heptose, a precursor for LPS inner core biosynthesis. RfaE is a bifunctional protein in E. coli, and separate proteins in some other genome. Domain I (TIGR02198) is suggested to act in D-glycero-D-manno-heptose 1-phosphate biosynthesis, while domain II (this family) adds ADP to yield ADP-D-glycero-D-manno-heptose. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 131254 [Multi-domain]  Cd Length: 144  Bit Score: 52.69  E-value: 2.06e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 374253760  171 GETVIYVAGAFDLFHIGHVDFLEKVHRLAERpyIIAGLHFDQEVNHYKGKNYPIMNLHERT--LSVLACryVSEVVI 245
Cdd:TIGR02199  10 GKKIVFTNGCFDILHAGHVSYLQQARALGDR--LVVGVNSDASVKRLKGETRPINPEEDRAevLAALSS--VDYVVI 82
G3P_Cytidylyltransferase cd02171
glycerol-3-phosphate cytidylyltransferase; Glycerol-3-phosphate cytidylyltransferase, ...
 172-268 3.69e-07

glycerol-3-phosphate cytidylyltransferase; Glycerol-3-phosphate cytidylyltransferase,(CDP-glycerol pyrophosphorylase). Glycerol-3-phosphate cytidyltransferase acts in pathways of teichoic acid biosynthesis. Teichoic acids are substituted polymers, linked by phosphodiester bonds, of glycerol, ribitol, etc. An example is poly(glycerol phosphate), the major teichoic acid of the Bacillus subtilis cell wall. Most, but not all, species encoding proteins in this family are Gram-positive bacteria. A closely related protein assigned a different function experimentally is a human ethanolamine-phosphate cytidylyltransferase.


Pssm-ID: 173922 [Multi-domain]  Cd Length: 129  Bit Score: 48.63  E-value: 3.69e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253760 172 ETVIYVAGAFDLFHIGHVDFLEKVHRLAErpYIIAGLHFDqEVNHYKGKNyPIMNLHERTLSVLACRYVSEVVIGAPYAV 251
Cdd:cd02171    1 MKVVITYGTFDLLHIGHLNLLERAKALGD--KLIVAVSTD-EFNAGKGKK-AVIPYEQRAEILESIRYVDLVIPETNWEQ 76

                         90
                 ....*....|....*..
gi 374253760 252 TAELLSHFKVDLVCHGK 268
Cdd:cd02171   77 KIEDIKKYNVDVFVMGD 93
PRK11316 PRK11316
bifunctional D-glycero-beta-D-manno-heptose-7-phosphate kinase/D-glycero-beta-D-manno-heptose ...
 171-236 4.40e-06

bifunctional D-glycero-beta-D-manno-heptose-7-phosphate kinase/D-glycero-beta-D-manno-heptose 1-phosphate adenylyltransferase HldE;


Pssm-ID: 183085 [Multi-domain]  Cd Length: 473  Bit Score: 48.29  E-value: 4.40e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 374253760 171 GETVIYVAGAFDLFHIGHVDFLEKVHRLAERpyIIAGLHFDQEVNHYKGKNYPIMNLhERTLSVLA 236
Cdd:PRK11316 339 GEKIVMTNGCFDILHAGHVSYLANARKLGDR--LIVAVNSDASVKRLKGEGRPVNPL-EQRMAVLA 401
G3P_Cytidylyltransferase cd02171
glycerol-3-phosphate cytidylyltransferase; Glycerol-3-phosphate cytidylyltransferase, ...
 11-90 2.30e-05

glycerol-3-phosphate cytidylyltransferase; Glycerol-3-phosphate cytidylyltransferase,(CDP-glycerol pyrophosphorylase). Glycerol-3-phosphate cytidyltransferase acts in pathways of teichoic acid biosynthesis. Teichoic acids are substituted polymers, linked by phosphodiester bonds, of glycerol, ribitol, etc. An example is poly(glycerol phosphate), the major teichoic acid of the Bacillus subtilis cell wall. Most, but not all, species encoding proteins in this family are Gram-positive bacteria. A closely related protein assigned a different function experimentally is a human ethanolamine-phosphate cytidylyltransferase.


Pssm-ID: 173922 [Multi-domain]  Cd Length: 129  Bit Score: 43.63  E-value: 2.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253760  11 VFTQEERYKMVQAIKWVDEVVPAAPYVTTLETLDKYNCDFCVHGNDITLTVDGRDTYEEVKqagrYREckRTQGVSTTDL 90
Cdd:cd02171   49 VIPYEQRAEILESIRYVDLVIPETNWEQKIEDIKKYNVDVFVMGDDWEGKFDFLKEYCEVV----YLP--RTKGISSTQL 122
cyt_tran_rel TIGR00125
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain ...
 2-30 2.63e-05

cytidyltransferase-like domain; Protein families that contain at least one copy of this domain include citrate lyase ligase, pantoate-beta-alanine ligase, glycerol-3-phosphate cytidyltransferase, ADP-heptose synthase, phosphocholine cytidylyltransferase, lipopolysaccharide core biosynthesis protein KdtB, the bifunctional protein NadR, and a number whose function is unknown. Many of these proteins are known to use CTP or ATP and release pyrophosphate.


Pssm-ID: 272920 [Multi-domain]  Cd Length: 66  Bit Score: 41.52  E-value: 2.63e-05
                          10        20
                  ....*....|....*....|....*....
gi 374253760    2 EIAKHKGPPVFTQEERYKMVQAIKWVDEV 30
Cdd:TIGR00125  38 FVNPLKGEPVFSLEERLEMLKALKYVDEV 66
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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